ID A0A0J0YEC0_9FLAO Unreviewed; 449 AA.
AC A0A0J0YEC0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=AB674_16965 {ECO:0000313|EMBL:KLT68521.1};
OS Flavobacterium sp. ABG.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423322 {ECO:0000313|EMBL:KLT68521.1, ECO:0000313|Proteomes:UP000036173};
RN [1] {ECO:0000313|EMBL:KLT68521.1, ECO:0000313|Proteomes:UP000036173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABG {ECO:0000313|EMBL:KLT68521.1,
RC ECO:0000313|Proteomes:UP000036173};
RA Gimbel A.B., Miller J.R., Newman J.D.;
RT "Flavobacterium sp. ABG.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLT68521.1}.
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DR EMBL; LEKS01000018; KLT68521.1; -; Genomic_DNA.
DR RefSeq; WP_047778464.1; NZ_LEKS01000018.1.
DR AlphaFoldDB; A0A0J0YEC0; -.
DR STRING; 1423322.AB674_16965; -.
DR PATRIC; fig|1423322.9.peg.3595; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000036173; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 130..170
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 449 AA; 48262 MW; 2A34FECE93605A93 CRC64;
MARFELKLPK MGESVAEATI TNWLKEVGDK IEADEAVLEI ATDKVDSEVP SEVTGILVER
LFGKDDLVQV GQVIAIIETE GGVETASSFL VDKIADEEST PAEATEIEKT IEGAKEAVAA
PQDFSTSEKF FSPLVKNIAK EEGVSVAELD SIQGSGKDGR VTKEDILKYI SDRKAGAVVA
PKAVVEPVKE VAAPKAAEPV VQKSQQAVPV SVNGGDEIIE MDRMRKLISG YMVASVQTSA
HVQSFIEVDV TNIVKWRDKV KTAFEKREGE KLTFTPIMME AVAKALKDFP GMNISVDGDY
IIKKKNINLG MAAALPNGNL IVPVIKNADQ LNLVGMAKAV NDLGGRAKAG KLKPDDTQGG
TYTVTNVGTF GSVFGTPIIN QPQVGILALG AIRKVPAVIE TPEGDFIGIR QKMFLSHSYD
HRVVDGALGG SFVKRVAEYL EAFDVNRDF
//
